Improving the thermostability and activity of Paenibacillus pasadenensis chitinase through semi-rational design

Xu, Pei; Ni, Zi-Fu; Zong, Min‐Hua; Ou, Xiao‐Yang; Yang, Juan; Lou, Wen‐Yong

doi:10.1016/j.ijbiomac.2020.02.033

Cited by 57 publications

(29 citation statements)

References 41 publications

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“…The thermostability of the chitinase enzyme can also be increased by site-directed mutagenesis and other molecular tools. Engineering of the Paenibacillus pasadenensis -derived chitinase PpChi1, by combinational mutagenesis and semi-rational design, improved the optimal temperature to 52.5 ℃, from 45 ℃ [ 45 ].…”

Section: Sources Of Chitinasesmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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Section: Sources Of Chitinasesmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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“…The sequence-specific structural-based mutation was employed to improve the thermostability of the chitinase enzyme. The specific mutants (S244C-I319C/T259P) were generated which showed a 26.3-fold increase in half-life at 122 • F with less libraries [62]. Through the semi-rational MD simulation predictive mode, the mutant had a stable active structure which was confirmed after generation of the mutation.…”

Section: Semi-rational Enzyme Engineering To Increase the Thermostabi...mentioning

confidence: 88%

A Review of Advanced Molecular Engineering Approaches to Enhance the Thermostability of Enzyme Breakers: From Prospective of Upstream Oil and Gas Industry

Naeem

Khalil

Tariq

et al. 2022

IJMS

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During the fracture stimulation of oil and gas wells, fracturing fluids are used to create fractures and transport the proppant into the fractured reservoirs. The fracturing fluid viscosity is responsible for proppant suspension, the viscosity can be increased through the incorporation of guar polymer and cross-linkers. After the fracturing operation, the fluid viscosity is decreased by breakers for efficient oil and gas recovery. Different types of enzyme breakers have been engineered and employed to reduce the fracturing fluid′s viscosity, but thermal stability remains the major constraint for the use of enzymes. The latest enzyme engineering approaches such as direct evolution and rational design, have great potential to increase the enzyme breakers’ thermostability against high temperatures of reservoirs. In this review article, we have reviewed recently advanced enzyme molecular engineering technologies and how these strategies could be used to enhance the thermostability of enzyme breakers in the upstream oil and gas industry.

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“…Plants and algae contain hemicellulose, a complex polymeric carbohydrate found in their cell walls. About 33% of the world's green organic carbon is made up of hemicellulose, which is composed primarily of xylan (Bhardwaj et al, 2019;Yang H. et al, 2020;Nwamba et al, 2021b;Shen et al, 2021;Sun et al, 2021). Hemicellulose is hydrolyzed by a variety of enzymes due to its heterogeneous structural composition (Zhuo et al, 2018).…”

Section: Xylanase Of Thermophilesmentioning

confidence: 99%

“…This mutant S244C-I319C/T259P with proline substitution and disulfide bond introduction exhibits increased specific activity at elevated temperatures as well as a 26.3-fold increase in halflife value at 50 °C. It also shows an increase in half-inactivation temperature with a 7.9 °C when compared to the wild type protein (Xu et al, 2020). A single point mutation was introduced into Penicillium canescens xylanase PcXylA, resulting in a 2.5-fold higher half-life at 50-60 °C (Denisenko et al, 2017).…”

Section: Semi-rational Designmentioning

confidence: 99%

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

Ajeje¹,

Hu²,

Song³

et al. 2021

Front. Bioeng. Biotechnol.

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The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

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Improving the thermostability and activity of Paenibacillus pasadenensis chitinase through semi-rational design

Cited by 57 publications

References 41 publications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

A Review of Advanced Molecular Engineering Approaches to Enhance the Thermostability of Enzyme Breakers: From Prospective of Upstream Oil and Gas Industry

Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

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